Related Experiment Video

Updated: Jun 6, 2026

Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo
10:35

Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo

Published on: February 5, 2021

Antibody dendrimers

Hiroyasu Yamaguchi1, Akira Harada

  • 1Department of Macromolecular Science, Graduate School of Science, Osaka University, Osaka, 560-0043, Japan.

Topics in Current Chemistry
|December 7, 2010
PubMed

Supramolecular formations of antibodies by their specific molecular recognition to antigens are investigated. Linear and network supramolecular architectures have been constructed by using immunoglobulin G (IgG) and divalent or trivalent antigens, respectively. An amplification method of the detection signals for the target molecule in the biosensors based on the surface plasmon resonance (SPR) has been devised using the signal enhancement in the supramolecular assembly of the antibody with multivalent antigens. Novel dendritic supramolecular complexes are designed and prepared by using immunoglobulin M (IgM) or protein A/G as a core and IgGs as branches. One of the "antibody dendrimers" is composed of proteins with a molecular weight of about 2 million and constructed by non-covalent bonds. The dendrimer can bind antigens strongly with high specificity. The biosensor technique based on SPR shows that the antibody dendrimer has the advantage of amplification of detection signals for antigens.

More Related Videos

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)09:39

Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)

Published on: September 17, 2019

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Antibody Actions01:26

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Cross-reactivity00:42

Cross-reactivity

Overview